5D-(5/6)-2,6-dihydroxy-5-(hydroxymethyl)cyclohex-2-en-1-one

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 5D-(5/6)-2,6-dihydroxy-5-(hydroxymethyl)cyclohex-2-en-1-one
• 英文别名: (5S,6S)-2,6-dihydroxy-5-(hydroxymethyl)cyclohex-2-en-1-one
• 化学式: C₇H₁₀O₄
• 分子量: 158.15
• InChiKey: JJEJEUFVVGEVHG-NJGYIYPDSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0
• 重原子数：
  11
• 可旋转键数：
  1
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.57
• 拓扑面积：
  77.8
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  4-Nitrophenyl-3-ketovalidamine 生成 4-硝基苯胺 、 5D-(5/6)-2,6-dihydroxy-5-(hydroxymethyl)cyclohex-2-en-1-one
  参考文献：
  名称：

  Purification and Properties of 3-Ketovalidoxylamine A C-N Lyase from Flavobacterium saccharophilum

  摘要：

  3-酮基戊二胺A C-N裂解酶通过硫酸铵分馏、CM纤维素柱色谱和Sephacryl S-200凝胶过滤从嗜糖黄杆菌的无细胞提取物中纯化约900倍。通过十二烷基硫酸钠（SDS）聚丙烯酰胺凝胶电泳判断，纯化的酶是均一的。通过Sephacryl S-200凝胶过滤和SDS聚丙烯酰胺凝胶电泳，估计酶的分子量为36,000，表明酶是一种单体。最佳pH值为9.0。EDTA或乙二醇双（β-氨基乙基醚）-N,N′-四乙酸抑制酶的活性，而Ca2+离子可逆转这种抑制作用。该酶能够从对硝基苯基-3-酮戊二胺（IV）或对硝基苯基-α-D-3-酮葡萄糖苷（VI）中消除对硝基苯胺或对硝基苯酚，但不能从对硝基苯基-1-表-3-酮戊二胺或对硝基苯基-β-D-3-酮葡萄糖苷中消除对硝基苯胺或对硝基苯酚。IV和VI的表观Km值分别为0.24 mM和0.5 mM。

  DOI：

  10.1093/oxfordjournals.jbchem.a135433

文献信息

• Microbial degradation of validamycin A by Flavobacterium saccharophilum. Enzymatic cleavage of C-N linkage in validoxylamine A.
  作者：NAOKI ASANO、MASAYOSHI TAKEUCHI、KOTARO NINOMIYA、YUKIHIKO KAMEDA、KATSUHIKO MATSUI

  DOI：10.7164/antibiotics.37.859

  日期：——

  The enzymatic cleavage of C-N linkage in the degradation of validamycin A by Flawbacterium saccharophilum was examined using N-p-nitrophenyl derivatives of validamine and valienamine as synthetic model substrates for validoxylamine A. Incubation of N-p-nitrophenylvalidamine with the membrane fraction from the organism led to formation of N-p-nitrophenyl-3-ketovalidamine, and succeeding cleavage of C-N linkage. As the products of the cleavage step, one was identified as p-nitroaniline and another keto compound could not be purified enough because of its instability. However, on the basis of its hydrogenation products, the structure of the keto compound could be established as 5D-(5/6)-5-C-(hydroxymethyl)-2, 6-dihydroxy-2-cyclohexen-1-one. The same experiment was carried out with N-p-nitrophenylvalienamine. In this case, N-p-nitrophenyl-3-ketovalienamine could be isolated as an intermediate but the desired keto compound from the cleavage step could not be isolated because of its instability. The participation of two enzymes, that is, a dehydrogenase and a C-N lyase on the cleavage of C-N linkage was assured, and moreover, the analysis of its products, together with those of the previous studies allow us to propose a degradation pathway of validamycin A by Flavobacteriwn saccharophilum.

  以N-对硝基苯基衍生物有效胺和缬胺作为有效氧胺A的合成模型底物，研究了嗜糖鞭毛霉降解有效霉素A过程中C-N连接的酶裂解。裂解步骤的产物中，一种被鉴定为对硝基苯胺，另一种酮化合物因其不稳定性而无法充分纯化。不过，根据其氢化产物，可以确定酮化合物的结构为 5D-(5/6)-5-C-（羟甲基）-2, 6-二羟基-2-环己烯-1-酮。对 N-对硝基苯缬烯胺也进行了同样的实验。在这种情况下，N-对硝基苯基-3-酮戊烯胺可以作为中间体分离出来，但由于其不稳定性，无法从裂解步骤中分离出所需的酮化合物。在 C-N 连接的裂解过程中，有两种酶（即脱氢酶和 C-N 裂解酶）的参与，此外，对其产物的分析以及先前研究的结果，使我们能够提出一种有效霉素 A 在黄杆菌（Flavobacteriwn saccharophilum）中的降解途径。
• Purification and Properties of 3-Ketovalidoxylamine A C-N Lyase from Flavobacterium saccharophilum
  作者：Masayoshi TAKEUCHI、Naoki ASANO、Yukihiko KAMEDA、Katsuhiko MATSUI

  DOI：10.1093/oxfordjournals.jbchem.a135433

  日期：1985.12

  3-Ketovalidoxylamine A C-N lyase was purified about 900-fold from the cell-free extract of Flavobacterium saccharophilum by animonium sulfate fractionation, column chromatography on CM cellulose and gel filtration on Sephacryl S-200. The purified enzyme was homogeneous as judged by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The molecular weight of the enzyme was estimated to be 36,000 by gel filtration on Sephacryl S-200 and by SDS polyacrylamide gel electrophoresis, indicating that the enzyme is a monomer. The optimum pH was found at 9.0. The enzyme activity was inhibited by EDTA or ethyleneglycol bis(β-aminoethylether)-N,N′-tetraacetic acid and the inhibition was reversed by Ca2+ ion. The enzyme was able to eliminate p-nitroaniline or p-nitrophenol from p-nitrophenyl-3-ketovalidamine (IV) or p-nitrophenyl-α-D-3-ketoglucoside (VI), but not from p-nitrophenyl-1-epi-3-ketovalidamine or p-nitrophenyl-β-D-3-ketoglucoside. Apparent Km values for IV and VI were 0.24 mM and 0.5 mM respectively.

  3-酮基戊二胺A C-N裂解酶通过硫酸铵分馏、CM纤维素柱色谱和Sephacryl S-200凝胶过滤从嗜糖黄杆菌的无细胞提取物中纯化约900倍。通过十二烷基硫酸钠（SDS）聚丙烯酰胺凝胶电泳判断，纯化的酶是均一的。通过Sephacryl S-200凝胶过滤和SDS聚丙烯酰胺凝胶电泳，估计酶的分子量为36,000，表明酶是一种单体。最佳pH值为9.0。EDTA或乙二醇双（β-氨基乙基醚）-N,N′-四乙酸抑制酶的活性，而Ca2+离子可逆转这种抑制作用。该酶能够从对硝基苯基-3-酮戊二胺（IV）或对硝基苯基-α-D-3-酮葡萄糖苷（VI）中消除对硝基苯胺或对硝基苯酚，但不能从对硝基苯基-1-表-3-酮戊二胺或对硝基苯基-β-D-3-酮葡萄糖苷中消除对硝基苯胺或对硝基苯酚。IV和VI的表观Km值分别为0.24 mM和0.5 mM。